5KS7

Crystal structure of Listeria monocytogenes OpuCA CBS domain dimer in complex with cyclic-di-AMP

5KS7 の概要

• エントリーDOI: 10.2210/pdb5ks7/pdb
• 関連するPDBエントリー: 5KS8
• 分子名称: Carnitine transport ATP-binding protein OpuCA, (2R,3R,3aS,5R,7aR,9R,10R,10aS,12R,14aR)-2,9-bis(6-amino-9H-purin-9-yl)octahydro-2H,7H-difuro[3,2-d:3',2'-j][1,3,7,9,2,8 ]tetraoxadiphosphacyclododecine-3,5,10,12-tetrol 5,12-dioxide (2 entities in total)
• 機能のキーワード: cbs domain, abc transporter, cyclic-di-amp, osmoregulation, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
• 由来する生物種: Listeria monocytogenes
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 29273.44

構造登録者

Choi, P.H.,Tong, L. (登録日: 2016-07-07, 公開日: 2016-07-20, 最終更新日: 2024-04-03)

主引用文献

Huynh, T.N.,Choi, P.H.,Sureka, K.,Ledvina, H.E.,Campillo, J.,Tong, L.,Woodward, J.J.
Cyclic di-AMP targets the cystathionine beta-synthase domain of the osmolyte transporter OpuC.
Mol.Microbiol., 102:233-243, 2016

PubMed Abstract: Cellular turgor is of fundamental importance to bacterial growth and survival. Changes in external osmolarity as a consequence of fluctuating environmental conditions and colonization of diverse environments can significantly impact cytoplasmic water content, resulting in cellular lysis or plasmolysis. To ensure maintenance of appropriate cellular turgor, bacteria import ions and small organic osmolytes, deemed compatible solutes, to equilibrate cytoplasmic osmolarity with the extracellular environment. Here, we show that elevated levels of c-di-AMP, a ubiquitous second messenger among bacteria, result in significant susceptibility to elevated osmotic stress in the bacterial pathogen Listeria monocytogenes. We found that levels of import of the compatible solute carnitine show an inverse correlation with intracellular c-di-AMP content and that c-di-AMP directly binds to the CBS domain of the ATPase subunit of the carnitine importer OpuC. Biochemical and structural studies identify conserved residues required for this interaction and transport activity in bacterial cells. Overall, these studies reveal a role for c-di-AMP mediated regulation of compatible solute import and provide new insight into the molecular mechanisms by which this essential second messenger impacts bacterial physiology and adaptation to changing environmental conditions.

PubMed: 27378384
DOI: 10.1111/mmi.13456

実験手法

X-RAY DIFFRACTION (2.9 Å)